Detect changes in secondary and tertiary structure
Today, the sensitivity and accuracy of Chirascan CD spectrometers reveals far more about changes that occur in the higher order structure (HOS) of proteins and other biomolecules when compared to the estimates of α-helix:β-sheet in secondary structure for which circular dichroism was first applied.
From confirming structural integrity to detecting minor changes in secondary and tertiary structure scientists can determine the effect of site-directed mutations on folding/unfolding (stability), monitor response to changes in temperature or pH, and reveal the effect of denaturing agents or binding partners.
Although providing less specific structural information when compared to X-ray crystallography or NMR spectroscopy (both give atomic resolution data), CD analysis offers a rapid analysis of proteins while in solution and requires relatively small amounts of sample.
By enabling the determination of structural and thermodynamic properties, each CD analysis leads to a deeper understanding of biomolecular characteristics, mechanisms and interactions
Gain insight and detect changes in secondary and tertiary structure
- Detect minor differences under native or stressed conditions
- Characterize protein stability
- Determine response to thermal or chemical changes
- Determine structural and thermodynamic properties
- Study folding and unfolding mechanisms
